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Biochemistry

Marquette University

Allosteric regulation

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Allosteric Regulation Of Pyruvate Carboxylase, Yumeng Liu Oct 2018

Allosteric Regulation Of Pyruvate Carboxylase, Yumeng Liu

Dissertations (1934 -)

Pyruvate carboxylase (PC; E.C.6.4.1.1) is a multifunctional, biotin-dependent enzyme that catalyzes the MgATP-dependent carboxylation of pyruvate to oxaloacetate. The overall reaction is accomplished by the coupling of two half reactions occurring at two spatially distinct catalytic domains by the translocation of a carrier domain, resulting in a net transfer of CO2 from bicarbonate to pyruvate. PC activity is regulated by multiple allosteric effectors with acetyl CoA serving as an activator in most species and L-aspartate serving as an inhibitor for microbial PC. The kinetic characterization of PC from different species have revealed that PC homologs are subject to divergent degrees …